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Lectin from Arachis hypogaea (peanut)

SIGMA/L7381 - FITC conjugate, lyophilized powder

Synonym: PNA; Peanut agglutinin

Product Type: Chemical

Catalog Number PKG Qty. Price Quantity
45-L7381-1MG 1 mg
$113.00
1/EA
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45-L7381-2MG 2 mg
$188.00
1/EA
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45-L7381-5MG 5 mg
$412.00
1/EA
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Agglutination
assay:
Lectin from Arachis hypogaea (peanut) (Cat. No.
L7381) at a concentration of ~1mg solid/mL was serially diluted (2-fold, top
to bottom of plate) and incubated with human erythrocytes type: O (4% v/v
RBC) to calculate Minimum agglutination titer (MAT). Agglutination is defined
as the inability of cells to form a tight button. PBS was used as blank.

 

composition Protein, ~10% Lowry
conjugate FITC conjugate
extent of labeling 4-8 mol FITC per mol protein
form lyophilized powder
Quality Level 200 
storage temp. −20°C
Application: Lectin from Arachis hypogaea (peanut) has been used:
• to determine the acrosomal status (presence or absence of acrosomal matrix corresponding to intact or acrosome-reacted spermatozoa) on viable sperm cells
• to probe cryosections of mediastinal lymph nodes (mLNs) with fluorochrome-labeled PNA and anti-B220 to detect germinal centers (GCs)
• to visualize the cone outer segments of pre-treated retinal sections

Biochem/physiol Actions: Lectin is known to be useful in glycoconjugate characterizing, imaging and targeting. Its use in a microarray assay, enable efficient glycome profiling. This is because of its specific interaction with oligosaccharides, glycoproteins and glycolipids. In plants and fungi, lectin defends against pathogens/feeders. Lectin participates in host recognition and tissue adhesion, thereby aids in the pathogenesis of microorganism.
Biochem/physiol Actions: PNA does not agglutinate normal human erythrocytes, but strongly agglutinates neuraminidase treated erythrocytes. PNA has potent anti-T activity similar to the anti-T antibody in human sera. The lectin can be used to distinguish between human lymphocyte subsets.
General description: Lectins are carbohydrate-binding proteins, omnipresent, found in fungi, plants and animals. The structure of lectin is diversely studied in plants and animals. The secondary structure of this protein is rich in β-strands and possesses a carbohydrate binding sites on the surface.
Packaging: 1, 2, 5 mg in glass bottle
Physical form: Contains phosphate buffer salts and NaCl
RIDADR NONH for all modes of transport
WGK Germany WGK 3
Flash Point(F) Not applicable
Flash Point(C) Not applicable
Storage Temp. −20°C
UNSPSC 12352202

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